Laminin interactions important for basement membrane assembly and possibly amyloidogenesis: Mapping the laminin binding site on the AA-amyloid precursor protein, apoSAA.

摘要

erum amyloid A isoforms, apoSAA1 and apoSAA2, are acute-phase proteins of unknown function and can be precursors of amyloid A peptides (AA) found in animal and human amyloid deposits. These deposits are often a complication of chronic-inflammatory disorders and are associated with a local disturbance in basement membrane (BM). As part of ongoing studies to understand the pathogenesis of this disease, I have found that laminin, a major BM glycoprotein, binds saturably, and with high affinity to several murine apoSAAs. These interactions involve a single class of binding sites which are ionic in nature, conformation dependent, and involve sulfhydryl groups. Laminin also bound with high affinity to 2 other potential amyloid precursors, apoA-I and